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CD209 antigen, widely known as DC-SIGN, is a type II transmembrane protein belonging to the C-type lectin family, predominantly expressed on dendritic cell subsets such as dermal dendritic cells and those in lymphoid tissues (UniProt P49760). It serves as a major pattern recognition receptor (PRR) that binds to mannose- and fucose-containing glycans on the surface of various pathogens, including HIV-1, Dengue virus, and Mycobacterium tuberculosis, facilitating their capture and subsequent antigen processing (Geijtenbeek et al., 2000). Additionally, DC-SIGN plays a vital role in cell-cell adhesion by interacting with ICAM-2 on vascular endothelium and ICAM-3 on T cells, which supports DC migration and the priming of naive T cells (Koppel et al., 2005). Because many viruses and bacteria exploit DC-SIGN to bypass immune defenses or disseminate throughout the host, it has become a focal point for therapeutic intervention. Current drug development efforts focus on glycomimetic compounds and monoclonal antibodies designed to block the carbohydrate recognition domain, thereby preventing pathogen attachment and modulating immune signaling pathways (Barchi, 2011).
Competitive inhibition of the carbohydrate recognition domain (CRD) to prevent pathogen binding and entry; Modulation of TLR-mediated signaling pathways
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